DPHS1_ARATH
ID DPHS1_ARATH Reviewed; 929 AA.
AC Q75QN6; F4KE97; Q9FFA8;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Dual specificity protein phosphatase PHS1;
DE EC=3.1.3.16;
DE EC=3.1.3.48;
DE AltName: Full=Protein PROPYZAMIDE-HYPERSENSITIVE 1;
GN Name=PHS1; OrderedLocusNames=At5g23720; ORFNames=MQM1.1;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ARG-64 AND CYS-792.
RX PubMed=15208393; DOI=10.1105/tpc.021865;
RA Naoi K., Hashimoto T.;
RT "A semidominant mutation in an Arabidopsis mitogen-activated protein kinase
RT phosphatase-like gene compromises cortical microtubule organization.";
RL Plant Cell 16:1841-1853(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP FUNCTION, AND INDUCTION BY ABSCISIC ACID.
RX PubMed=16889651; DOI=10.1111/j.1365-313x.2006.02823.x;
RA Quettier A.L., Bertrand C., Habricot Y., Miginiac E., Agnes C.,
RA Jeannette E., Maldiney R.;
RT "The phs1-3 mutation in a putative dual-specificity protein tyrosine
RT phosphatase gene provokes hypersensitive responses to abscisic acid in
RT Arabidopsis thaliana.";
RL Plant J. 47:711-719(2006).
RN [6]
RP FUNCTION, INTERACTION WITH MPK18, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP ARG-64.
RX PubMed=19392697; DOI=10.1111/j.1365-313x.2009.03895.x;
RA Walia A., Lee J.S., Wasteneys G., Ellis B.;
RT "Arabidopsis mitogen-activated protein kinase MPK18 mediates cortical
RT microtubule functions in plant cells.";
RL Plant J. 59:565-575(2009).
RN [7]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF LEU-906 AND
RP LEU-909.
RX PubMed=20224945; DOI=10.1007/s00425-010-1135-8;
RA Pytela J., Kato T., Hashimoto T.;
RT "Mitogen-activated protein kinase phosphatase PHS1 is retained in the
RT cytoplasm by nuclear extrusion signal-dependent and independent
RT mechanisms.";
RL Planta 231:1311-1322(2010).
CC -!- FUNCTION: Probable dual specificity phosphatase that binds and
CC dephosphorylates MPK18, modulating the organization and dynamics of
CC cortical microtubules. Acts as negative regulator of abscisic acid
CC (ABA) signaling during seed germination and light-induced stomata
CC aperture. {ECO:0000269|PubMed:15208393, ECO:0000269|PubMed:16889651,
CC ECO:0000269|PubMed:19392697}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044};
CC -!- SUBUNIT: Interacts with MPK18. {ECO:0000269|PubMed:19392697}.
CC -!- INTERACTION:
CC Q75QN6; Q9C5C0: MPK18; NbExp=3; IntAct=EBI-2349366, EBI-1238534;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19392697,
CC ECO:0000269|PubMed:20224945}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q75QN6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q75QN6-2; Sequence=VSP_043502;
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves and flowers.
CC {ECO:0000269|PubMed:15208393, ECO:0000269|PubMed:20224945}.
CC -!- INDUCTION: By abscisic acid. {ECO:0000269|PubMed:16889651}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality when homozygous in the phs1-2
CC allele (PubMed:15208393), but after several backcrossing, phs1-2 and
CC other homozygous alleles (phs1-4 and phs1-5) are similar to the wild-
CC type (PubMed:20224945). {ECO:0000269|PubMed:15208393,
CC ECO:0000269|PubMed:20224945}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB10045.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB161693; BAD18373.1; -; mRNA.
DR EMBL; AB005244; BAB10045.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB025633; BAB10045.1; JOINED; Genomic_DNA.
DR EMBL; CP002688; AED93202.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93203.1; -; Genomic_DNA.
DR RefSeq; NP_197761.2; NM_122277.2. [Q75QN6-2]
DR RefSeq; NP_851066.2; NM_180735.4. [Q75QN6-1]
DR AlphaFoldDB; Q75QN6; -.
DR SMR; Q75QN6; -.
DR BioGRID; 17712; 5.
DR IntAct; Q75QN6; 2.
DR STRING; 3702.AT5G23720.1; -.
DR iPTMnet; Q75QN6; -.
DR PaxDb; Q75QN6; -.
DR PRIDE; Q75QN6; -.
DR ProteomicsDB; 220300; -. [Q75QN6-1]
DR EnsemblPlants; AT5G23720.1; AT5G23720.1; AT5G23720. [Q75QN6-1]
DR EnsemblPlants; AT5G23720.2; AT5G23720.2; AT5G23720. [Q75QN6-2]
DR GeneID; 832437; -.
DR Gramene; AT5G23720.1; AT5G23720.1; AT5G23720. [Q75QN6-1]
DR Gramene; AT5G23720.2; AT5G23720.2; AT5G23720. [Q75QN6-2]
DR KEGG; ath:AT5G23720; -.
DR Araport; AT5G23720; -.
DR TAIR; locus:2171691; AT5G23720.
DR eggNOG; KOG1716; Eukaryota.
DR OMA; RDYRSIQ; -.
DR OrthoDB; 1576308at2759; -.
DR PhylomeDB; Q75QN6; -.
DR PRO; PR:Q75QN6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q75QN6; baseline and differential.
DR Genevisible; Q75QN6; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0016301; F:kinase activity; IEA:InterPro.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:TAIR.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0043622; P:cortical microtubule organization; IMP:TAIR.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR GO; GO:0010468; P:regulation of gene expression; IMP:TAIR.
DR GO; GO:0010119; P:regulation of stomatal movement; IMP:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR CDD; cd05124; AFK; 1.
DR Gene3D; 1.10.1070.11; -; 1.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR015275; Actin-fragmin_kin_cat_dom.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR035010; PHS1.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR PANTHER; PTHR47100; PTHR47100; 1.
DR Pfam; PF09192; Act-Frag_cataly; 1.
DR Pfam; PF00782; DSPc; 1.
DR SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Alternative splicing; Cytoplasm;
KW Hydrolase; Protein phosphatase; Reference proteome.
FT CHAIN 1..929
FT /note="Dual specificity protein phosphatase PHS1"
FT /id="PRO_0000417331"
FT DOMAIN 703..848
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 903..911
FT /note="Nuclear export signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 545..561
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..609
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 792
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT BINDING 792..798
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..89
FT /note="MAEPEKKRDQPFSQEKDEEKDLYLVHDEHESPLPLTVTSRVLYMLGDIASGP
FT AYRFTQWLDLVRKRSATYGSSGFPHRLHRIDDMVTSA -> MIWSL (in isoform
FT 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_043502"
FT MUTAGEN 64
FT /note="R->C: In phs1-1; reduces activity 2-fold. Primary
FT roots skewing. No effect on the interaction with MPK18."
FT /evidence="ECO:0000269|PubMed:15208393,
FT ECO:0000269|PubMed:19392697"
FT MUTAGEN 792
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:15208393"
FT MUTAGEN 906
FT /note="L->A: Loss of nuclear export; when associated with
FT A-909."
FT /evidence="ECO:0000269|PubMed:20224945"
FT MUTAGEN 909
FT /note="L->A: Loss of nuclear export; when associated with
FT A-906."
FT /evidence="ECO:0000269|PubMed:20224945"
SQ SEQUENCE 929 AA; 104235 MW; 5FE10C006DD39A07 CRC64;
MAEPEKKRDQ PFSQEKDEEK DLYLVHDEHE SPLPLTVTSR VLYMLGDIAS GPAYRFTQWL
DLVRKRSATY GSSGFPHRLH RIDDMVTSAG ERNTDPKSPP SRQSSEISLW ERLGKASTVD
IDSSCFSWNM LSSLHHTEHS SSTDHSEEDQ SKPLEVTVNS GGVVFFALFN SSSSEDASRK
EEAAVIKFAS SRMATQSERL GYEFSKWLGV QIPQARVIHS CNPEWTLIKE ATEKAQAKAT
SEGDEVGEMT CSELLEALEL SRCLLLMSYV HGCPMLESMS SFETEEKAER AAAALGRILV
LDLVIRNEDR LPCRQLRWRG NPANLLLTDR IVSSAKHHEC SFDEAFDSAI KRYHPKDYRS
IQRERRASSV DSRSRLSISD QMLVSQASDF SDITESPRSY DTGLMSPMSD RSVAADFHLV
AIDSGVPRRP PAGKRASDQE IYPRLVELLL NSSQYSSNLL HEITEGSLGY PQAEDGEETS
NVRSVVTPVV REFRNGFRAG LRDLQEFHIF LVTLHQKLDV LLRAFFSMMD KTMCADFDRE
DFAVPESPSH THGHEVNHYP SPSKDRVPSD NSSDHSESDM QKSVPRTPNS ENKEDGSSPK
SRESWHGRSG KGGESLSSQR LAAKLRDFHK FAKVDAESNK ELDQWNETLR NEVMKLCQEN
GFNTGFFEGS DNNSCTDAYE LKVRLEHILE RISLISKAAN TEKPSMIQEN LFIGGGLAAR
SIYTLQHLGI THVLCLCANE IGQSDTQYPD LFEYQNFSIT DDEDSNIESI FQEALDFIKH
GEETGGKILV HCFEGRSRSA TVVLAYLMLQ KKLTLLEAWS KLRKVHRRAQ PNDGFARILI
NLDKKCHGKV SMEWRQRKPT MKVCPVCGKN AGLSSSSLKL HLQKSHRKLS SGSVDSAMNM
EIQKALEALK LSTGRGSSAS SNSFQSHPG
